ID Q5YGK5_9MARC Unreviewed; 381 AA.
AC Q5YGK5;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
DE Flags: Fragment;
GN Name=atpB {ECO:0000313|EMBL:AAS89136.1};
OS Porella navicularis.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAS89136.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Jungermanniopsida; Jungermanniidae; Porellales; Porellineae; Porellaceae;
OC Porella.
OX NCBI_TaxID=269545 {ECO:0000313|EMBL:AAS89136.1};
RN [1] {ECO:0000313|EMBL:AAS89136.1}
RP NUCLEOTIDE SEQUENCE.
RA Forrest L.L., Crandall-Stotler B.J.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAS89136.1}
RP NUCLEOTIDE SEQUENCE.
RA Forrest L.L., Crandall-Stotler B.J.;
RT "A phylogeny of the simple thalloid liverworts (Jungermanniopsida, subclass
RT Metzgeriidae) as inferred from five chloroplast genes.";
RL (In) Goffinet B., Hollowell V., Magill R. (eds.);
RL MOLECULAR SYSTEMATICS OF BRYOPHYTES: MONOGRAPHS IN SYSTEMATIC BOTANY FROM
RL THE MISSOURI BOTANICAL GARDEN SERIES (VOL. 98), pp.119-140, Missouri
RL Botanical Garden Press, St. Louis, MO, USA (2004).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001741,
CC ECO:0000256|RuleBase:RU003553};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC subunits: a(1), b(1), b'(1) and c(9-12).
CC {ECO:0000256|RuleBase:RU003553}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY507377; AAS89136.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YGK5; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003553};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW Chloroplast {ECO:0000313|EMBL:AAS89136.1};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000313|EMBL:AAS89136.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 58..250
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAS89136.1"
FT NON_TER 381
FT /evidence="ECO:0000313|EMBL:AAS89136.1"
SQ SEQUENCE 381 AA; 41599 MW; 611EC079AD0D4C21 CRC64;
LWKIFNVLGE PVDNLGPVDA GTTFPIHRSA PAFTQLDTKL SIFETGIKVV DLLAPYRRGG
KIGLFGGAGV GKTVLIMELI NNIAKAHGGV SVFGGVGERT REGNDLYMEM KESKVINEQN
ISESKVALVY GQMNEPPGAR MRVGLTALTM AEYFRDINKQ DVLLFIDNIF RFVQAGSEVS
ALLGRMPSAV GYQPTLSTEM GTLQERITST KEGSITSIQA VYVPADDLTD PAPATTFAHL
DATTVLSRGL AAKGIYPAVD PLDSTSTMLQ PWIVGEEHYE TAQGVKQTLQ RYKELQDIIA
ILGLDELSEE DRLTVARARK IERFLSQPFF VAEVFTGSPG KYVSLRETIK GFQMILSGEL
DNLPEQAFYL VGNIDEVTAK A
//
